SECD_MYCLE
ID SECD_MYCLE Reviewed; 571 AA.
AC P38387; O69485; Q9CCT3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=ML0487;
GN ORFNames=B1177_C1_164, MLCB1259.05;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 88-571.
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC the SecYEG preprotein conducting channel. SecDF uses the proton motive
CC force (PMF) to complete protein translocation after the ATP-dependent
CC function of SecA. {ECO:0000255|HAMAP-Rule:MF_01463}.
CC -!- SUBUNIT: Forms a complex with SecF. Part of the essential Sec protein
CC translocation apparatus which comprises SecA, SecYEG and auxiliary
CC proteins SecDF. Other proteins may also be involved.
CC {ECO:0000255|HAMAP-Rule:MF_01463}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01463};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01463}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01463}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17086.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAC29995.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL023591; CAA19080.1; -; Genomic_DNA.
DR EMBL; AL583918; CAC29995.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00011; AAA17086.1; ALT_FRAME; Genomic_DNA.
DR PIR; G86969; G86969.
DR PIR; S72722; S72722.
DR RefSeq; NP_301427.2; NC_002677.1.
DR RefSeq; WP_010907751.1; NC_002677.1.
DR AlphaFoldDB; P38387; -.
DR SMR; P38387; -.
DR STRING; 272631.ML0487; -.
DR EnsemblBacteria; CAC29995; CAC29995; CAC29995.
DR KEGG; mle:ML0487; -.
DR PATRIC; fig|272631.5.peg.851; -.
DR Leproma; ML0487; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_2_11; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01463_B; SecD_B; 1.
DR InterPro; IPR005791; SecD.
DR InterPro; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
DR InterPro; IPR022646; SecD/SecF_CS.
DR PANTHER; PTHR30081; PTHR30081; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR TIGRFAMs; TIGR01129; secD; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..571
FT /note="Protein translocase subunit SecD"
FT /id="PRO_0000095965"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT REGION 124..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 60719 MW; 40852F70E049B496 CRC64;
MASSSAPVHF GRYLSMFLVL FIGVYLLAFL TGDKRVVPRL GIDLQGGTRV TLTARTPDGS
RPSREALSQA QQIISSRVNG LGVSGSEVVV DGDNLVITVP GNDGNEARNL GQTARLYIRP
VLNSLPVQRG QDPKPGSPAG TLPNFAPMPP DHPGAQPRPY LQDPTSSPSS DPMPSPVPTG
AALPGEVPSV EQPAPPDPRK DLAERIAEEK KWRQSTKQSI QFLALQFEST HCDKDDILAG
NDDPNLPLAT CSTDHNMAYL LAPSIISGDQ IQNSTSGMNQ RGVGYVVDLQ FKSAAADVWA
DFTAAHIGTQ TAFTLDSEVV SVPVINEAIL GGRTQISGGD PPFTAATARQ LANVLKYGSL
PLSFEPSEAQ TVSATLGLTS LRAGLIAGAI GLSLVLLYSL LYYRVLGLLT AFSLFCSGTI
IFAILVLLGR YINYTLDLAG IAGLIIGIGT TADSFVVFFE RIKDEIREGR SFRSAVPRGW
VRARKTIVSG NAVTFLAAAV LHFLAIGQVK GFAFTLGLTT ILDLVVVFLV TWPLVYLASK
SPLLARPAYN GLGAVQQVAR ERRASAKTGR G
